http://www.cnr.it/ontology/cnr/individuo/prodotto/ID47730
The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes: an update (Articolo in rivista)
- Type
- Label
- The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes: an update (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/mas.20090 (literal)
- Alternative label
Annunziata Lapolla; Domenico Fedele; Roberta Seraglia;Pietro Traldi (2006)
The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes: an update
in Mass spectrometry reviews (Print); John Wiley & Sons, Ltd., New York (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Annunziata Lapolla; Domenico Fedele; Roberta Seraglia;Pietro Traldi (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://onlinelibrary.wiley.com/doi/10.1002/mas.20090/abstract (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1,2 : Dipartimento di Scienze Mediche e Chirurgiche, Cattedra di Malattie del Metabolismo, Universita` di Padova, Padova, Italy /
3,4 : CNR-ISTM, Corso Stati Uniti 4, Padova, Italy (literal)
- Titolo
- The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes: an update (literal)
- Abstract
- Recent studies on non-enzymatic protein glycation are
reviewed, and results are critically discussed. Advanced glycation
end products (AGE) levels in the body reflect a balance
between their formation and catabolism. AGE proteolysis leads
to the formation of low-molecular-weight AGE (AGE peptides)
that are normally excreted in urine. In the case of diabetic disease
and/or renal failure, AGE peptides accumulate in plasma.
Because of their high reactivity, these compounds have been
thought to play a role in the progression of chronic complications.
The structural identification of these compounds is particularly
important, and a strategy has been designed for their possible
definition. A series of experiments has been devoted to the
study of the enzymatic degradation products of in vitro glycated
human serum albumin (HSA). This approach, based on different
MS methods (LC/ESI/MS, LC/ESI/FTMS, MALDI), led to the
detection of the glycated peptides generated by digestion of
HSA. A further study was devoted to the possible identification
of the peptides identified in the glycated HSA digestion products
in the plasma of diabetic and nephropatic subjects. No glycated
HSA digestion products were found in plasma samples of the
subjects under investigation even if clear differences were found
among the LC runs from populations of healthy, diabetic, and
nephropatic subjects. Parallel investigations were devoted to
the evaluation of glyoxal and methylglyoxal-dicarbonyl compounds
that originate at the intermediate stage of the Maillard
reaction. This evaluation was performed in diabetic patients,
before and after the achievement of good metabolic control,
and in nephropatic patients subjected to peritoneal dialysis
(PD). In the latter case, results indicated that these dicarbonyl
compounds, already present in the dialysis fluids, show a
decrease in plasma and in dialysis fluids; those data suggested
their reaction at peritoneal membrane level. (literal)
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